FN Archimer Export Format
PT J
TI Characterization of a small tRNA ‐binding protein that interacts with the archaeal proteasome complex
BT 
AF Hogrel, Gaëlle
   Marino‐Puertas, Laura
   Laurent, Sebastien
   Ibrahim, Ziad
   Covès, Jacques
   Girard, Eric
   Gabel, Frank
   Fenel, Daphna
   Daugeron, Marie‐Claire
   Clouet‐d'Orval, Béatrice
   Basta, Tamara
   Flament, Didier
   Franzetti, Bruno
AS 1:1;2:1;3:2;4:1;5:1;6:1;7:1;8:1;9:3;10:4;11:3;12:2;13:1;
FF 1:;2:;3:PDG-REM-BEEP-LMEE;4:;5:;6:;7:;8:;9:;10:;11:;12:PDG-REM-BEEP-LMEE;13:;
C1 CNRS, CEA, IBS Univ Grenoble Alpes Grenoble, France
   Univ Brest, Ifremer, CNRS, Laboratoire de Microbiologie des Environnements Extrêmes, F 29280, Plouzané, France
   Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS Université Paris‐Saclay Gif‐sur‐Yvette, France
   Laboratoire de Microbiologie et de Génétique Moléculaires, UMR5100, Centre de Biologie Intégrative (CBI) Université de Toulouse, CNRS, Université Paul Sabatier Toulouse, France
C2 CNRS, FRANCE
   IFREMER, FRANCE
   UNIV PARIS SACLAY, FRANCE
   UNIV TOULOUSE, FRANCE
SI BREST
SE PDG-REM-BEEP-LMEE
UM BEEP-LM2E
IN WOS Ifremer UMR
   copubli-france
   copubli-univ-france
IF 3.6
TC 0
UR https://archimer.ifremer.fr/doc/00779/89070/94625.pdf
   https://archimer.ifremer.fr/doc/00779/89070/94626.docx
LA English
DT Article
DE ;Archaea;OB-fold;proteasome;protein-protein interaction;ribosome-associated quality control;tRNA binding
AB The proteasome system allows the elimination of functional or structurally impaired proteins. This includes the degradation of nascent peptides. In Archaea, how the proteasome complex interacts with the translational machinery remains to be described. Here, we characterized a small orphan protein, Q9UZY3 (UniProt ID), conserved in Thermococcales. The protein was identified in native pull-down experiments using the proteasome regulatory complex (proteasome-activating nucleotidase [PAN]) as bait. X-ray crystallography and small-angle X-ray scattering experiments revealed that the protein is monomeric and adopts a β-barrel core structure with an oligonucleotide/oligosaccharide-binding (OB)-fold, typically found in translation elongation factors. Mobility shift experiment showed that Q9UZY3 displays transfer ribonucleic acid (tRNA)-binding properties. Pull-downs, co-immunoprecipitation and isothermal titration calorimetry (ITC) studies revealed that Q9UZY3 interacts in vitro with PAN. Native pull-downs and proteomic analysis using different versions of Q9UZY3 showed that the protein interacts with the assembled PAN–20S proteasome machinery in Pyrococcus abyssi (Pa) cellular extracts. The protein was therefore named Pbp11, for Proteasome-Binding Protein of 11 kDa. Interestingly, the interaction network of Pbp11 also includes ribosomal proteins, tRNA-processing enzymes and exosome subunits dependent on Pbp11's N-terminal domain that was found to be essential for tRNA binding. Together these data suggest that Pbp11 participates in an interface between the proteasome and the translational machinery. 
PY 2022
PD JUN
SO Molecular Microbiology
SN 0950-382X
PU Wiley
VL 118
IS 1-2
UT 000811147500001
BP 16
EP 29
DI 10.1111/mmi.14948
ID 89070
ER

EF